Please use this identifier to cite or link to this item: https://doi.org/10.3390/molecules26195909
DC FieldValue
dc.titleAnti-fungal hevein-like peptides biosynthesized from quinoa cleavable hololectins
dc.contributor.authorLoo, Shining
dc.contributor.authorTay, Stephanie, V
dc.contributor.authorKam, Antony
dc.contributor.authorTang, Fan
dc.contributor.authorFan, Jing-Song
dc.contributor.authorYang, Daiwen
dc.contributor.authorTam, James P.
dc.date.accessioned2022-10-13T07:32:41Z
dc.date.available2022-10-13T07:32:41Z
dc.date.issued2021-09-29
dc.identifier.citationLoo, Shining, Tay, Stephanie, V, Kam, Antony, Tang, Fan, Fan, Jing-Song, Yang, Daiwen, Tam, James P. (2021-09-29). Anti-fungal hevein-like peptides biosynthesized from quinoa cleavable hololectins. Molecules 26 (19) : 5909. ScholarBank@NUS Repository. https://doi.org/10.3390/molecules26195909
dc.identifier.issn1420-3049
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/233121
dc.description.abstractChitin-binding hevein-like peptides (CB-HLPs) belong to a family of cysteine-rich peptides that play important roles in plant stress and defense mechanisms. CB-HLPs are ribosomally synthesized peptides that are known to be bioprocessed from the following two types of three-domain CB-HLP precursor architectures: cargo-carrying and non-cargo-carrying. Here, we report the identification and characterization of chenotides biosynthesized from the third type of precursors, which are cleavable hololectins of the quinoa (Chenopodium quinoa) family. Chenotides are 6-Cys-CB-HLPs of 29–31 amino acids, which have a third type of precursor architecture that encompasses a canonical chitin-binding domain that is involved in chitin binding and anti-fungal activities. Microbroth dilution assays and microscopic analyses showed that chenotides are effective against phyto-pathogenic fungi in the micromolar range. Structure determination revealed that chenotides are cystine knot-ted and highly compact, which could confer resistance against heat and proteolytic degradation. Importantly, chenotides are connected by a novel 18-residue Gly/Ala-rich linker that is a target for bioprocessing by cathepsin-like endopeptidases. Taken together, our findings reveal that chenotides are a new family of CB-HLPs from quinoa that are synthesized as a single multi-modular unit and bioprocessed to yield individual mature CB-HLPs. Importantly, such precursors constitute a new family of cleavable hololectins. This unusual feature could increase the biosynthetic efficiency of anti-fungal CB-HLPs, to provide an evolutionary advantage for plant survival and reproduction. © 2021 by the authors. Licensee MDPI, Basel, Switzerland.
dc.publisherMDPI
dc.rightsAttribution 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.sourceScopus OA2021
dc.subjectAnti-fungal
dc.subjectChitin
dc.subjecthevein-like peptide
dc.subjectHololectin
dc.subjectLinker
dc.subjectQuinoa
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.3390/molecules26195909
dc.description.sourcetitleMolecules
dc.description.volume26
dc.description.issue19
dc.description.page5909
Appears in Collections:Staff Publications
Elements

Show simple item record
Files in This Item:
File Description SizeFormatAccess SettingsVersion 
10_3390_molecules26195909.pdf3.83 MBAdobe PDF

OPEN

NoneView/Download

Google ScholarTM

Check

Altmetric


This item is licensed under a Creative Commons License Creative Commons